ID A0A2Y9IS70_ENHLU Unreviewed; 862 AA.
AC A0A2Y9IS70;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=DNA topoisomerase {ECO:0000256|ARBA:ARBA00012891, ECO:0000256|RuleBase:RU362092};
DE EC=5.6.2.1 {ECO:0000256|ARBA:ARBA00012891, ECO:0000256|RuleBase:RU362092};
GN Name=LOC111142472 {ECO:0000313|RefSeq:XP_022351362.1,
GN ECO:0000313|RefSeq:XP_022351363.1, ECO:0000313|RefSeq:XP_022351364.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022351363.1};
RN [1] {ECO:0000313|RefSeq:XP_022351362.1, ECO:0000313|RefSeq:XP_022351363.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022351362.1,
RC ECO:0000313|RefSeq:XP_022351363.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Introduces a single-strand break via transesterification at a
CC target site in duplex DNA. Releases the supercoiling and torsional
CC tension of DNA introduced during the DNA replication and transcription
CC by transiently cleaving and rejoining one strand of the DNA duplex. The
CC scissile phosphodiester is attacked by the catalytic tyrosine of the
CC enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme
CC intermediate and the expulsion of a 3'-OH DNA strand.
CC {ECO:0000256|RuleBase:RU362092}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-independent breakage of single-stranded DNA, followed by
CC passage and rejoining.; EC=5.6.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000213,
CC ECO:0000256|RuleBase:RU362092};
CC -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC {ECO:0000256|ARBA:ARBA00009446, ECO:0000256|RuleBase:RU362092}.
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DR RefSeq; XP_022351362.1; XM_022495654.1.
DR RefSeq; XP_022351363.1; XM_022495655.1.
DR RefSeq; XP_022351364.1; XM_022495656.1.
DR STRING; 391180.A0A2Y9IS70; -.
DR KEGG; elk:111142472; -.
DR OrthoDB; 166270at2759; -.
DR Proteomes; UP000248482; Unplaced.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity; IEA:UniProtKB-EC.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR CDD; cd00186; TOP1Ac; 1.
DR CDD; cd03362; TOPRIM_TopoIA_TopoIII; 1.
DR Gene3D; 3.40.50.140; -; 1.
DR Gene3D; 1.10.460.10; Topoisomerase I, domain 2; 1.
DR Gene3D; 2.70.20.10; Topoisomerase I, domain 3; 1.
DR Gene3D; 1.10.290.10; Topoisomerase I, domain 4; 1.
DR InterPro; IPR000380; Topo_IA.
DR InterPro; IPR003601; Topo_IA_2.
DR InterPro; IPR023406; Topo_IA_AS.
DR InterPro; IPR013497; Topo_IA_cen.
DR InterPro; IPR013824; Topo_IA_cen_sub1.
DR InterPro; IPR013825; Topo_IA_cen_sub2.
DR InterPro; IPR013826; Topo_IA_cen_sub3.
DR InterPro; IPR023405; Topo_IA_core_domain.
DR InterPro; IPR003602; Topo_IA_DNA-bd_dom.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034144; TOPRIM_TopoIII.
DR PANTHER; PTHR11390:SF20; DNA TOPOISOMERASE 3-BETA-1; 1.
DR PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 1.
DR Pfam; PF01131; Topoisom_bac; 1.
DR Pfam; PF01751; Toprim; 1.
DR PRINTS; PR00417; PRTPISMRASEI.
DR SMART; SM00437; TOP1Ac; 1.
DR SMART; SM00436; TOP1Bc; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SUPFAM; SSF56712; Prokaryotic type I DNA topoisomerase; 1.
DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU362092};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU362092};
KW Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW ECO:0000256|RuleBase:RU362092}.
FT DOMAIN 3..153
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 821..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..844
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 862 AA; 96608 MW; D56EFFAC960BADC1 CRC64;
MRTVLMVAEK PSLAQSIAKI LSRGNMSSHK GLNGTCSVHE YSGTFAGQAV RFKMTSVCGH
VMTLDFLGKY NKWDKVDPAE LFSQAPTEKK EANPKLNMVK FLQVEGKGCD YIVLWLDCDK
EGENICFEVL DAVLPVMNPA HGGEKTVFRA RFSSITDTDI CAAMARLGEP DHNEALSVDA
RQELDLRIGC AFTRFQTKYF QGKYGNLDSS LISFGPCQTP TLGFCVERHD KIQSFKPETY
WVLQAKVNAD KDRSLLLDWD RVRVFDREIA QMFLNMTKLE KEAQVEATSR KEKAKQRPLA
LNTVEMLRVA SSSLGMGPQH AMQTAERLYT QGYISYPRTE TTHYPENFDL KGPLRQQANH
PYWADTVKRL LAEGINRPRK GHDAGDHPPI TPMRSATEAE LGGEAWRLYE YITRHFIATV
SYDCKYLQST IAFRIGPEHF TCTGKTVISP GFTEIMPWQS VPLEESLPTC QRGDTFPVSE
IKLLEKQTSP PDYLTEAELI TLMEKHGIGT DASIPVHINN ICQRNYVTVE SGRRLKPTNL
GIVLVHGYYK IDAELVLPTI RSAVEKQLNL IAQGKADYRQ VLGHTLDVFK RKFHYFVDSI
AGMDELMEVS FSPLAATGKP LSRCGKCHRF MKYIQAKPSR LHCSHCDETY TLPQNGTIKL
YKELRCPLDD FELVLWSSGS RGKSYPLCPY CSNHPPFRDM KKGMGCNECT HPTCQHSLSM
LGIGQCVGCE GGVLVLDPTS GPKWKVACNK CNVVAHCFEN AYRVRVSADT CRTCEAALLA
VDFNKAKSPL PGDETQHTGC VFCDPIFQEL VELKHAASCH PMHRGGPGRR QGRGRARGRR
PPGKPSARRP KDKMSALAAY FV
//
